ABSTRACT
The lipoprotein (lpp) gene codes for the most abundant protein in bacteria and its nucleic acid sequence has been determined. The structure of the chemically synthesized double-stranded DNA fragment used to join the lpp promoter and ribosome-binding site to the Human growth hormone (hGH) coding region. A hGH comprises a single polypeptide chain of 191 amino acids with a molecular weight of 22,000. This hormone is limiting for linear growth in man and it also has a number of other biological activities. Expression of methionyl hGH by the bacterium harboring pNM736 was found to be as high as that for pNM645. That methionyl hGH, rather than hGH, was actually made was verified by comparing the properties of the bacterially synthesized material with that of authentic hGH with the use of high pressure liquid chromatography. The methionyl hGH was partially purified from 500 gm of E. coli.
